Two 3D experiments, (H)CCH 3 -TOCSY and H(C)CH 3 -TOCSY, are proposed for resonance assignment of methyl-containing amino acid side chains. After the initial proton-carbon INEPT step, during which either carbon or proton chemical shift labeling is achieved (t 1 ), the magnetization is spread along t
A 4D HCCH-TOCSY experiment for assigning the side chain1H and13C resonances of proteins
✍ Scribed by Edward T. Olejniczak; Robert X. Xu; Stephen W. Fesik
- Publisher
- Springer Netherlands
- Year
- 1992
- Tongue
- English
- Weight
- 268 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0925-2738
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
A 3D triple resonance experiment has been designed to provide intraresidual and sequential correlations between amide nitrogens and c~-carbons in uniformly 13C/15N-labeled proteins. In-phase 13C~ magnetization is transferred to the aliphatic side-chain protons via the side-chain carbons using a CC-T
In paramagnetic heme proteins, it is often problematic to make the reduced (usually diamagnetic) state lack isotropic shifts proton resonance assignments for heme substituents that do not and are therefore difficult to examine by NMR spectroscopy. have large isotropic shifts and consequently lie und